ID   F4C3G0_SPHS2            Unreviewed;       297 AA.
AC   F4C3G0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ADZ78138.1};
GN   OrderedLocusNames=Sph21_1576 {ECO:0000313|EMBL:ADZ78138.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78138.1};
RN   [1] {ECO:0000313|EMBL:ADZ78138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ78138.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
CC       {ECO:0000256|ARBA:ARBA00037183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00001141};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002584; ADZ78138.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C3G0; -.
DR   STRING; 743722.Sph21_1576; -.
DR   KEGG; shg:Sph21_1576; -.
DR   PATRIC; fig|743722.3.peg.1691; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_6_4_10; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:ADZ78138.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ADZ78138.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..248
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   297 AA;  33472 MW;  D172C0994AECEA2F CRC64;
     MSPAYAGLFL FNSFIKIFIF AGIAKDLVEN AMVEPLIHEI SCRIGYTKTA YLHMNKFFGY
     ILTPFHYLYF GLILVIFHPI QWICLKLGGY EAHKRSVDIL NWFLTSSYYL LGNSVHFINN
     QQLPVAQPII FIANHQSMYD IPPLIYFLRK HHAKFVSKIE LASGIPSISF NLKYGGAANI
     DRSDPKQSIA EILKLAKNMK DKNWSTVIFP EGTRSKTGVM KPFAVGGIAT ILKKVPHAII
     VPVVINNSWK MVQYGSFPLR AFTAMSWEVL APISSEGRTA EDVVKAAEEA IREKVVP
//